KPYK1_YEAST
ID KPYK1_YEAST Reviewed; 500 AA.
AC P00549; D6VPH8; Q2VQG5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Pyruvate kinase 1;
DE Short=PK 1;
DE EC=2.7.1.40 {ECO:0000269|PubMed:10413488};
DE AltName: Full=cell division cycle protein 19;
GN Name=CDC19; Synonyms=PYK1; OrderedLocusNames=YAL038W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2653861; DOI=10.1016/0014-5793(89)81359-6;
RA McNally T., Purvis I.J., Fothergill-Gilmore L.A., Brown A.L.P.;
RT "The yeast pyruvate kinase gene does not contain a string of non-preferred
RT codons: revised nucleotide sequence.";
RL FEBS Lett. 247:312-316(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6185493; DOI=10.1016/s0021-9258(18)32907-7;
RA Burke R.L., Tekamp-Olson P., Najarian R.;
RT "The isolation, characterization, and sequence of the pyruvate kinase gene
RT of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 258:2193-2201(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76625 / YPH499, Ba194, Bb32, Fy93, M1-2A, M2-8, M5-7A, M5-7B,
RC M7-8D, MMR2-1, MMR2-3, MMR2-5, MMW1-12, MMW1-15, MMW1-15h2, MMW1-2,
RC MMW1-2h2, ORM1-1, Sgu52E, Sgu52F, YPS396, YPS400, YPS598, YPS600, YPS602,
RC YPS604, YPS606, YPS608, and YPS610;
RX PubMed=16879422; DOI=10.1111/j.1567-1364.2006.00059.x;
RA Aa E., Townsend J.P., Adams R.I., Nielsen K.M., Taylor J.W.;
RT "Population structure and gene evolution in Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 6:702-715(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF LYS-240.
RX PubMed=10413488; DOI=10.1021/bi990690n;
RA Bollenbach T.J., Mesecar A.D., Nowak T.;
RT "Role of lysine 240 in the mechanism of yeast pyruvate kinase catalysis.";
RL Biochemistry 38:9137-9145(1999).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND THR-478, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-213, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-16; THR-31; SER-70;
RP THR-184; SER-316; SER-450 AND THR-478, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-204; LYS-255 AND LYS-446, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG;
RP FRUCTOSE-1-6-DIPHOSPHATE; MANGANESE IONS AND POTASSIUM IONS.
RX PubMed=9519410; DOI=10.1016/s0969-2126(98)00021-5;
RA Jurica M.S., Mesecar A., Heath P.J., Shi W., Nowak T., Stoddard B.L.;
RT "The allosteric regulation of pyruvate kinase by fructose-1,6-
RT bisphosphate.";
RL Structure 6:195-210(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000269|PubMed:10413488};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10413488};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000305|PubMed:9519410};
CC -!- ACTIVITY REGULATION: The activity is regulated by glucose levels.
CC Activated by fructose-1,6-bisphosphate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.31 mM for phosphoenolpyruvate (with magnesium as divalent
CC cation) {ECO:0000269|PubMed:10413488};
CC KM=0.021 mM for phosphoenolpyruvate (with manganese as divalent
CC cation) {ECO:0000269|PubMed:10413488};
CC KM=1.10 mM for ADP (with magnesium as divalent cation)
CC {ECO:0000269|PubMed:10413488};
CC KM=0.24 mM for ADP (with manganese as divalent cation)
CC {ECO:0000269|PubMed:10413488};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:10413488};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- MISCELLANEOUS: Present with 291000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; V01321; CAA24631.1; -; Genomic_DNA.
DR EMBL; X14400; CAA32573.1; -; Genomic_DNA.
DR EMBL; AY949862; AAY27264.1; -; Genomic_DNA.
DR EMBL; AY949863; AAY27265.1; -; Genomic_DNA.
DR EMBL; AY949864; AAY27266.1; -; Genomic_DNA.
DR EMBL; AY949865; AAY27267.1; -; Genomic_DNA.
DR EMBL; AY949866; AAY27268.1; -; Genomic_DNA.
DR EMBL; AY949867; AAY27269.1; -; Genomic_DNA.
DR EMBL; AY949868; AAY27270.1; -; Genomic_DNA.
DR EMBL; AY949869; AAY27271.1; -; Genomic_DNA.
DR EMBL; AY949870; AAY27272.1; -; Genomic_DNA.
DR EMBL; AY949871; AAY27273.1; -; Genomic_DNA.
DR EMBL; AY949872; AAY27274.1; -; Genomic_DNA.
DR EMBL; AY949873; AAY27275.1; -; Genomic_DNA.
DR EMBL; AY949874; AAY27276.1; -; Genomic_DNA.
DR EMBL; AY949875; AAY27277.1; -; Genomic_DNA.
DR EMBL; AY949876; AAY27278.1; -; Genomic_DNA.
DR EMBL; AY949877; AAY27279.1; -; Genomic_DNA.
DR EMBL; AY949878; AAY27280.1; -; Genomic_DNA.
DR EMBL; AY949879; AAY27281.1; -; Genomic_DNA.
DR EMBL; AY949880; AAY27282.1; -; Genomic_DNA.
DR EMBL; AY949881; AAY27283.1; -; Genomic_DNA.
DR EMBL; AY949882; AAY27284.1; -; Genomic_DNA.
DR EMBL; AY949883; AAY27285.1; -; Genomic_DNA.
DR EMBL; AY949884; AAY27286.1; -; Genomic_DNA.
DR EMBL; AY949885; AAY27287.1; -; Genomic_DNA.
DR EMBL; AY949886; AAY27288.1; -; Genomic_DNA.
DR EMBL; AY949887; AAY27289.1; -; Genomic_DNA.
DR EMBL; AY949888; AAY27290.1; -; Genomic_DNA.
DR EMBL; AY949889; AAY27291.1; -; Genomic_DNA.
DR EMBL; AY949890; AAY27292.1; -; Genomic_DNA.
DR EMBL; U12980; AAC04993.1; -; Genomic_DNA.
DR EMBL; AY693107; AAT93126.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06948.1; -; Genomic_DNA.
DR PIR; S05764; KIBYP.
DR RefSeq; NP_009362.1; NM_001178183.1.
DR PDB; 1A3W; X-ray; 3.00 A; A/B=1-500.
DR PDB; 1A3X; X-ray; 3.00 A; A/B=1-500.
DR PDBsum; 1A3W; -.
DR PDBsum; 1A3X; -.
DR AlphaFoldDB; P00549; -.
DR SMR; P00549; -.
DR BioGRID; 31727; 321.
DR DIP; DIP-4124N; -.
DR ELM; P00549; -.
DR IntAct; P00549; 186.
DR MINT; P00549; -.
DR STRING; 4932.YAL038W; -.
DR MoonProt; P00549; -.
DR CarbonylDB; P00549; -.
DR iPTMnet; P00549; -.
DR COMPLUYEAST-2DPAGE; P00549; -.
DR MaxQB; P00549; -.
DR PaxDb; P00549; -.
DR PRIDE; P00549; -.
DR TopDownProteomics; P00549; -.
DR EnsemblFungi; YAL038W_mRNA; YAL038W; YAL038W.
DR GeneID; 851193; -.
DR KEGG; sce:YAL038W; -.
DR SGD; S000000036; CDC19.
DR VEuPathDB; FungiDB:YAL038W; -.
DR eggNOG; KOG2323; Eukaryota.
DR GeneTree; ENSGT00390000008859; -.
DR HOGENOM; CLU_015439_0_1_1; -.
DR InParanoid; P00549; -.
DR OMA; QVPIVQK; -.
DR BioCyc; YEAST:YAL038W-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-70171; Glycolysis.
DR SABIO-RK; P00549; -.
DR UniPathway; UPA00109; UER00188.
DR EvolutionaryTrace; P00549; -.
DR PRO; PR:P00549; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P00549; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IDA:SGD.
DR GO; GO:0006096; P:glycolytic process; IMP:SGD.
DR GO; GO:0006090; P:pyruvate metabolic process; IMP:SGD.
DR CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 1.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; ATP-binding; Glycolysis;
KW Isopeptide bond; Kinase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Potassium; Pyruvate;
KW Reference proteome; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CHAIN 2..500
FT /note="Pyruvate kinase 1"
FT /id="PRO_0000112121"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3X"
FT BINDING 51..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 51
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT BINDING 53
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT BINDING 84
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT BINDING 85
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3X"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT BINDING 402..407
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W"
FT BINDING 452
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT BINDING 459
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT BINDING 484
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000269|PubMed:9519410,
FT ECO:0007744|PDB:1A3W, ECO:0007744|PDB:1A3X"
FT SITE 240
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:10413488"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 184
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 478
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 446
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 240
FT /note="K->M: Reduces activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:10413488"
FT CONFLICT 382..386
FT /note="VAASA -> SLPR (in Ref. 1; CAA24631)"
FT /evidence="ECO:0000305"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1A3X"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:1A3W"
FT TURN 116..120
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1A3W"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:1A3W"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1A3X"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:1A3W"
FT TURN 333..337
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 341..355
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1A3X"
FT HELIX 361..368
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 378..393
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 406..413
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:1A3W"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:1A3W"
FT HELIX 455..469
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:1A3W"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:1A3W"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:1A3W"
SQ SEQUENCE 500 AA; 54545 MW; 78D753FC410C5820 CRC64;
MSRLERLTSL NVVAGSDLRR TSIIGTIGPK TNNPETLVAL RKAGLNIVRM NFSHGSYEYH
KSVIDNARKS EELYPGRPLA IALDTKGPEI RTGTTTNDVD YPIPPNHEMI FTTDDKYAKA
CDDKIMYVDY KNITKVISAG RIIYVDDGVL SFQVLEVVDD KTLKVKALNA GKICSHKGVN
LPGTDVDLPA LSEKDKEDLR FGVKNGVHMV FASFIRTAND VLTIREVLGE QGKDVKIIVK
IENQQGVNNF DEILKVTDGV MVARGDLGIE IPAPEVLAVQ KKLIAKSNLA GKPVICATQM
LESMTYNPRP TRAEVSDVGN AILDGADCVM LSGETAKGNY PINAVTTMAE TAVIAEQAIA
YLPNYDDMRN CTPKPTSTTE TVAASAVAAV FEQKAKAIIV LSTSGTTPRL VSKYRPNCPI
ILVTRCPRAA RFSHLYRGVF PFVFEKEPVS DWTDDVEARI NFGIEKAKEF GILKKGDTYV
SIQGFKAGAG HSNTLQVSTV
